CN102559722A - Heatproof aldolase gene with high enzyme activity, aldolase, carrier, engineering bacteria and application - Google Patents
Heatproof aldolase gene with high enzyme activity, aldolase, carrier, engineering bacteria and application Download PDFInfo
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- CN102559722A CN102559722A CN2012100640278A CN201210064027A CN102559722A CN 102559722 A CN102559722 A CN 102559722A CN 2012100640278 A CN2012100640278 A CN 2012100640278A CN 201210064027 A CN201210064027 A CN 201210064027A CN 102559722 A CN102559722 A CN 102559722A
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- aldolase
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- ala
- zymohexase
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Abstract
The invention provides an aldolase gene, aldolase coded by the gene, a carrier containing the gene, engineering bacteria and application of the gene. The gene is from Pyrococcus kodakaraensis. The nucleotide sequence of the aldolase gene (DERA) is shown in the SEQ ID NO.1 and the amino acid sequence of aldolase is shown in the SEQ ID NO.2. Aldolase can be used for synthesizing 2,4,6-tri-deoxyhexamethylose compounds, is environment-friendly and has broad application prospect.
Description
(1) technical field
The present invention relates to a kind of aldolase gene, and the zymohexase of this genes encoding, and the carrier, engineering bacteria and the application thereof that contain this gene.
(2) background technology
Zymohexase is as the enzyme of the three-dimensional Cheng Jian of catalyzed carbon carbon atom; Can be applied in widely organic chemistry synthetic in; That can be starting point easily with the small molecules carry out asymmetry catalysis to big complicated molecule direction is synthetic for it, and this process is that meaning is particularly outstanding in the reaction of substrate at glucide.Use the high regioselectivity of enzyme, can avoid the protection to the active hydroxyl in the glucide easily, more outstanding is can introduce new chiral centre at catalyzed carbon carbon bond synthetic while zymohexase.This just ability that can efficiently introduce chiral carbon atom; Make zymohexase in the synthetic field of drug molecule, have a wide range of applications, compare to have clear superiority with chemical technology; As: avoided the use of hazardous and noxious substances, synthetic can under normal temperature and pressure conditions, carrying out.From substituting the angle of traditional chemical synthesis technique catalyzer, this enzymatic reaction has very strong green attribute, the Green Chemistry transformation of traditional chemical technology is had significance, thereby this enzyme has broad application prospects.
(3) summary of the invention
The purpose of this invention is to provide a kind of aldolase gene, the zymohexase of this genes encoding, and the carrier, engineering bacteria and the application thereof that contain this gene.
The technical scheme that the present invention adopts is:
A kind of aldolase gene (DERA) that derives from Pyrococcus kodakaraensis, its nucleotide sequence is shown in SEQ ID NO.1:
atgaacaaac gtgaaattgc acgttacatt gatcagacca acctgaaacc atacgcgact 60
aaagaagata tcatcaagct gtgtgatgaa gcgatcgaat acggctttta cgccgtttgc 120
gtgaacccgt accgtgtgaa gctggcgaaa gactatctgc gtgaaaagaa tgctgatgtt 180
aaagtagcat ctgttatcgg tttcccgctg ggcgccaccc cgaccgaagt taaagttttc 240
gaagccaaac gtgctctgga agatggtgca gacgagctgg acatggttat caacatcggc 300
gcgctgaaag ataaagacta tgaatatgtt aagaacgaca tcgcagaagt ggttaaagta 360
gcgcacgaac gcggcgctaa agtgaaagta attatcgaaa cttgctacct gaccgaagag 420
gagaaagtga aagcgtgtga gctggccaaa gaggcgggtg ctgacttcgt taagactagc 480
accggtttcg gtaccggtgg tgctaccgtg gaagacgtgc gtctgatgcg caaagtggtt 540
ggcccggaaa tgggcgtaaa agcagctggt ggtattcgca cctatgaaca ggctctggag 600
atgatcgaag caggtgcgaa ccgtatcggc acctcctctg gcgtaaaaat tgtagaaggt 660
gcgccggacg aactcgag 678
Because the singularity of nucleotide sequence, the variant of polynucleotide shown in any SEQ NO:1 as long as itself and this polynucleotide have 90% above homology, all belongs to the row of protection domain of the present invention.The variant of said polynucleotide is meant a kind of polynucleotide sequence that one or more Nucleotide change that has.The variant of these polynucleotide can make the living allelic variant or the varient of non-life, comprises replacing varient, deletion mutation body and inserting varient.As known in the art, allelic variant is the replacement form of polynucleotide, and it possibly be replacement, disappearance or the insertion of a plurality of Nucleotide, but can be from not changing the function of its amino acids coding in fact.
A kind of high enzyme is lived, heat-stable zymohexase, by said aldolase gene coding.Concrete, said zymohexase aminoacid sequence is shown in SEQ ID NO.2:
Met Asn Lys Arg Glu Ile Ala Arg Tyr Ile Asp Gln Thr Asn Leu Lys
1 5 10 15
Pro Tyr Ala Thr Lys Glu Asp Ile Ile Lys Leu Cys Asp Glu Ala Ile
20 25 30
Glu Tyr Gly Phe Tyr Ala Val Cys Val Asn Pro Tyr Arg Val Lys Leu
35 40 45
Ala Lys Asp Tyr Leu Arg Glu Lys Asn Ala Asp Val Lys Val Ala Ser
50 55 60
Val Ile Gly Phe Pro Leu Gly Ala Thr Pro Thr Glu Val Lys Val Phe
65 70 75 80
Glu Ala Lys Arg Ala Leu Glu Asp Gly Ala Asp Glu Leu Asp Met Val
85 90 95
Ile Asn Ile Gly Ala Leu Lys Asp Lys Asp Tyr Glu Tyr Val Lys Asn
100 105 110
Asp Ile Ala Glu Val Val Lys Val Ala His Glu Arg Gly Ala Lys Val
115 120 125
Lys Val Ile Ile Glu Thr Cys Tyr Leu Thr Glu Glu Glu Lys Val Lys
130 135 140
Ala Cys Glu Leu Ala Lys Glu Ala Gly Ala Asp Phe Val Lys Thr Ser
145 150 155 160
Thr Gly Phe Gly Thr Gly Gly Ala Thr Val Glu Asp Val Arg Leu Met
165 170 175
Arg Lys Val Val Gly Pro Glu Met Gly Val Lys Ala Ala Gly Gly Ile
180 185 190
Arg Thr Tyr Glu Gln Ala Leu Glu Met Ile Glu Ala Gly Ala Asn Arg
195 200 205
Ile Gly Thr Ser Ser Gly Val Lys Ile Val Glu Gly Ala Pro Asp Glu
210 215 220
Leu Glu
225
Has high temperature resistant, high enzyme than the characteristic of living through the protein that experiment showed, said structure.
Because the singularity of aminoacid sequence; Any fragment or its variant that contains the polypeptide of aminoacid sequence shown in the SEQ NO.2; Like its examples of conservative variations, bioactive fragment or verivate; As long as the fragment of this polypeptide or polypeptide variants and aforementioned amino acid sequence homology all belong to the row of protection domain of the present invention more than 95%.Concrete, said change can comprise amino acid whose disappearance, insertion or replacement in the aminoacid sequence; Wherein, for the conservative property change of variant, the amino acid of being replaced has structure similar with original acid or chemical property, and as replacing Isoleucine with leucine, variant also can have non-conservation and change, as replacing glycocoll with tryptophane.
The invention still further relates to a kind of recombinant vectors that contains said aldolase gene, and said recombinant vectors transforms the recombination engineering bacteria that obtains.
The invention still further relates to the application of described aldolase gene in preparation reorganization zymohexase.
Concrete; Described being applied as: make up the recombinant vectors that contains said aldolase gene; Said recombinant vectors is converted in the intestinal bacteria, and the recombination engineering bacteria of acquisition carries out inducing culture (being inductor usually with IPTG), and nutrient solution separates and to obtain containing the somatic cells of zymohexase of recombinating.
Main points of the present invention have been to provide the aminoacid sequence shown in nucleotide sequence shown in the SEQ NO.1 and the SEQ NO.2; Under the situation of known this nucleotide sequence and aminoacid sequence; The acquisition of this nucleotide sequence and aminoacid sequence; And the acquisition of relevant recombinant vectors, genetic engineering bacterium, all be conspicuous to those skilled in the art.
High enzyme of the present invention is lived, heat-stable zymohexase can obtain as follows:
1, the synthetic and clone of the cDNA of DERA full length gene: according to the nucleotide sequence of DERA gene, carry out full gene and synthesize, obtain the aldolase gene of the nucleotide sequence shown in the SEQ ID NO.1.
2, the structure that contains the expression vector of goal gene: the aldolase gene that step 1 is obtained is cloned into intermediate carrier.
3, the recombinant expression vector that step 2 is obtained changes in the host cell, like intestinal bacteria (Escherichia coli) BL 21, under the condition that is fit to the expression zymohexase, cultivates said host cell.
4, from the culture of step 3, isolate zymohexase.
Beneficial effect of the present invention is mainly reflected in: a kind of zymohexase is provided, and the gene of this zymohexase of encoding, carrier, engineering bacteria and application thereof, this zymohexase can be used for 2,4,6-three deoxyhexamethylose compounds synthetic, and environmental protection has a extensive future.
(4) description of drawings
Fig. 1 is the zymohexase expression of results (M:marker of Pyrococcus kodakaraensis; 2: whole cell albumen; 3:DERA).
Fig. 2 be in the reaction of DERA cracking 2-deoxy-D-ribose-5-SULPHOSUCCINIC ACID ESTER NADH at the 340nm place light absorption value change curve.
Fig. 3 is the relative vigor of DERA after the treatment of different temperature.
(5) embodiment
Below in conjunction with specific embodiment the present invention is described further, but protection scope of the present invention is not limited in this:
Synthetic and the clone of the cDNA of embodiment 1:DERA full length gene
According to the nucleotide sequence among the NCBI from the DERA gene of Pyrococcus kodakaraensis, hand in the sea and give birth to worker's biotechnology ltd to carry out full gene synthetic, successfully obtain the sequence of Nucleotide shown in the SEQ ID NO.1.According to the DERA gene coded sequence (SEQ ID NO.1) of Pyrococcus kodakaraensis, design amplifies the primer that complete coding is read frame, and on the upstream and downstream primer, introduces restriction endonuclease sites respectively, so that expression vector.With gene synthetic product is template; Behind pcr amplification; The DERA of Pyrococcus kodakaraensis is cloned into intermediate carrier pET303/CT (available from Invitrogen company); Guaranteeing to identify good expression vector under the correct prerequisite of reading frame, again it is changed among the E.Coil BL21, obtain engineering bacteria E.Coil BL21/pET 303CT/DERA.
The proteic expression of embodiment 2:DERA
With the E.Coil BL21/pET 303CT/DERA shaking table incubated overnight in the LB liquid nutrient medium that contains 100mL100 μ g/mL penbritin that obtains among the embodiment 1.Bacterium liquid after the 10ml incubated overnight is poured into the LB liquid nutrient medium of 1L 100 μ g/mL penbritins and cultivated, up to bacterium liquid OD
600Reach at 0.6～0.8 o'clock adding the IPTG final concentration is 0.5mM, 28 ℃ induce 16h after, centrifugal collection thalline, thalline makes its resuspension with 25ml phosphoric acid buffer pH7.4, the ultrasonication cell.Centrifuging and taking supernatant, the supernatant that contains DERA with 0.22 μ m FM membrane filtration after nickel post affinity chromatography carry out purifying and obtain the pure enzyme of DERA.Comprehensive BCA method zymoprotein concentration determination data, the expression amount of DERA enzyme reaches 56mg/L (Fig. 1) in the LB substratum.
The ratio enzyme activity determination of embodiment 3:DERA
The present invention is a substrate with 2-deoxy-D-ribose-5-SULPHOSUCCINIC ACID ESTER; Under the room temperature condition; DERA catalytic pyrolysis a part substrate is separated and is obtained a part glyceraldehyde 3-phosphate; It is under the situation of NADH and triose-phosphate isomerase existence, and by the catalysis of glycerine triphosphoric acid desaturase, each molecule glyceraldehyde 3-phosphate is consumed a part NADH by catalysis.Absorb at the UV of 340nm wavelength through measuring N ADH and to detect the natural substrate degrading activity of kinetic curve with assay determination DERA.The decomposition of the corresponding a part 2-of the consumption of a part NADH deoxy-D-ribose-5-SULPHOSUCCINIC ACID ESTER.
Concrete operations are following: DERA is made into enzyme liquid with 100mM trolamine damping fluid (pH8.0) dissolving; Be added to mixing solutions (the 0.1mM NADH of substrate; 0.4mM 2-deoxy-D-ribose-5-SULPHOSUCCINIC ACID ESTER, 11U/mL triose-phosphate isomerase, 4U/mL glycerine triphosphoric acid desaturase); Measure 340nm place light absorption value, per second is measured once.The speed that goes out the variation of NADH light absorption value according to the preceding 100 seconds data computation of curve is :-0.024min
-1(Fig. 2).The used enzyme amount of primary first-order equation is 5 μ L, and enzyme concn is determined as 12.5ng/ μ L through the BCA method, and the specific activity of enzyme that draws DERA according to above data computation is: 31.27U/mg has higher specific activity of enzyme.
The thermostability of embodiment 4:DERA
To use enzyme liquid that 100mM trolamine damping fluid (pH8.0) dissolving DERA is made into respectively at 20 ℃, 30 ℃, 40 ℃, 50 ℃; 60 ℃, 70 ℃, 80 ℃, 90 ℃; 100 ℃ of warm down 10min that bathe mix with reaction solution described in the embodiment 3 afterwards, measure the decomposition vigor down in 50 ℃.The decomposition vigor of measuring under the same conditions with untreated DERA is 100%, and the DERA that obtains after each Temperature Treatment decomposes vigor relatively.As shown in Figure 3, the result shows the higher thermostability of DERA enzyme tool from Pyrococcus kodakaraensis.
SEQUENCE LISTING
< 110>Hangzhou Pedagogic University
< 120>a kind of high enzyme work, heat-resisting aldolase gene, enzyme, carrier, engineering bacteria and application
<130>
<160> 2
<170> PatentIn version 3.4
<210> 1
<211> 678
<212> DNA
<213> Pyrococcus kodakaraensis
<400> 1
atgaacaaac gtgaaattgc acgttacatt gatcagacca acctgaaacc atacgcgact 60
aaagaagata tcatcaagct gtgtgatgaa gcgatcgaat acggctttta cgccgtttgc 120
gtgaacccgt accgtgtgaa gctggcgaaa gactatctgc gtgaaaagaa tgctgatgtt 180
aaagtagcat ctgttatcgg tttcccgctg ggcgccaccc cgaccgaagt taaagttttc 240
gaagccaaac gtgctctgga agatggtgca gacgagctgg acatggttat caacatcggc 300
gcgctgaaag ataaagacta tgaatatgtt aagaacgaca tcgcagaagt ggttaaagta 360
gcgcacgaac gcggcgctaa agtgaaagta attatcgaaa cttgctacct gaccgaagag 420
gagaaagtga aagcgtgtga gctggccaaa gaggcgggtg ctgacttcgt taagactagc 480
accggtttcg gtaccggtgg tgctaccgtg gaagacgtgc gtctgatgcg caaagtggtt 540
ggcccggaaa tgggcgtaaa agcagctggt ggtattcgca cctatgaaca ggctctggag 600
atgatcgaag caggtgcgaa ccgtatcggc acctcctctg gcgtaaaaat tgtagaaggt 660
gcgccggacg aactcgag 678
<210> 2
<211> 226
<212> PRT
<213> Pyrococcus kodakaraensis
<400> 2
Met Asn Lys Arg Glu Ile Ala Arg Tyr Ile Asp Gln Thr Asn Leu Lys
1 5 10 15
Pro Tyr Ala Thr Lys Glu Asp Ile Ile Lys Leu Cys Asp Glu Ala Ile
20 25 30
Glu Tyr Gly Phe Tyr Ala Val Cys Val Asn Pro Tyr Arg Val Lys Leu
35 40 45
Ala Lys Asp Tyr Leu Arg Glu Lys Asn Ala Asp Val Lys Val Ala Ser
50 55 60
Val Ile Gly Phe Pro Leu Gly Ala Thr Pro Thr Glu Val Lys Val Phe
65 70 75 80
Glu Ala Lys Arg Ala Leu Glu Asp Gly Ala Asp Glu Leu Asp Met Val
85 90 95
Ile Asn Ile Gly Ala Leu Lys Asp Lys Asp Tyr Glu Tyr Val Lys Asn
100 105 110
Asp Ile Ala Glu Val Val Lys Val Ala His Glu Arg Gly Ala Lys Val
115 120 125
Lys Val Ile Ile Glu Thr Cys Tyr Leu Thr Glu Glu Glu Lys Val Lys
130 135 140
Ala Cys Glu Leu Ala Lys Glu Ala Gly Ala Asp Phe Val Lys Thr Ser
145 150 155 160
Thr Gly Phe Gly Thr Gly Gly Ala Thr Val Glu Asp Val Arg Leu Met
165 170 175
Arg Lys Val Val Gly Pro Glu Met Gly Val Lys Ala Ala Gly Gly Ile
180 185 190
Arg Thr Tyr Glu Gln Ala Leu Glu Met Ile Glu Ala Gly Ala Asn Arg
195 200 205
Ile Gly Thr Ser Ser Gly Val Lys Ile Val Glu Gly Ala Pro Asp Glu
210 215 220
Leu Glu
225
Claims (7)
1. aldolase gene that derives from Pyrococcus kodakaraensis, its nucleotide sequence is shown in SEQ ID NO.1.
2. one kind high alive, the heat-stable zymohexase of enzyme is encoded by the said aldolase gene of claim 1.
3. zymohexase as claimed in claim 2 is characterized in that said zymohexase aminoacid sequence is shown in SEQID NO.2.
4. recombinant vectors that contains the said aldolase gene of claim 1.
5. one kind transforms the recombination engineering bacteria that obtains with the said recombinant vectors of claim 4.
6. the application of aldolase gene as claimed in claim 1 in preparation reorganization zymohexase.
7. application as claimed in claim 6; It is characterized in that described being applied as: make up the recombinant vectors that contains said aldolase gene; Said recombinant vectors is converted in the intestinal bacteria; The recombination engineering bacteria that obtains carries out inducing culture, and nutrient solution separates and obtains containing the somatic cells of zymohexase of recombinating.
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108103083A (en) * | 2017-12-13 | 2018-06-01 | 江苏省原子医学研究所 | Nucleotide sequence, expression vector, engineering bacteria and the production recombined human aldolase C method of encoding recombinant human's aldolase C |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101443446A (en) * | 2006-03-07 | 2009-05-27 | 维莱尼姆公司 | Aldolases, nucleic acids encoding them and methods for making and using them |
| CN101921790A (en) * | 2010-05-19 | 2010-12-22 | 杭州师范大学 | Aldolase gene, enzyme, vector, engineering bacterium and application thereof |
| CN101921789A (en) * | 2010-05-19 | 2010-12-22 | 杭州师范大学 | Aldolase, coding gene, carrier, engineering bacterium and application thereof |
| CN102329764A (en) * | 2010-03-23 | 2012-01-25 | 杭州师范大学 | Recombinant heat-resistant aldolase genetically engineered strain and application thereof |
-
2012
- 2012-03-12 CN CN201210064027.8A patent/CN102559722B/en active Active
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101443446A (en) * | 2006-03-07 | 2009-05-27 | 维莱尼姆公司 | Aldolases, nucleic acids encoding them and methods for making and using them |
| CN102329764A (en) * | 2010-03-23 | 2012-01-25 | 杭州师范大学 | Recombinant heat-resistant aldolase genetically engineered strain and application thereof |
| CN101921790A (en) * | 2010-05-19 | 2010-12-22 | 杭州师范大学 | Aldolase gene, enzyme, vector, engineering bacterium and application thereof |
| CN101921789A (en) * | 2010-05-19 | 2010-12-22 | 杭州师范大学 | Aldolase, coding gene, carrier, engineering bacterium and application thereof |
Non-Patent Citations (5)
| Title |
|---|
| ETSUKO N. MORIYAMA ET AL.: "Gene length and codon usage bias in Drosophila melanogaster, Saccharomyces cerevisiae and Escherichia coli", 《NUCLEIC ACIDS RESEARCH》 * |
| FUKUI,T. ET AL.: "deoxyribose-phosphate aldolase [Thermococcus kodakarensis KOD1]", 《NCBI GENBANK，YP_184517.1》 * |
| HENGJIANG DONG ET AL.: "Co-variation of tRNA Abundance and Codon Usage in Escherichia coli at Different Growth Rates", 《J. MOL. BIOL》 * |
| PAUL M.SHARP AND WEN-HSIUNG LI: "Codon usage in regulatory genes in Escherichia coli does not reflect selection for "rare" codons", 《NUCLEIC ACIDS RESEARCH》 * |
| 解庭波: "大肠杆菌表达系统的研究进展", 《长江大学学报》 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108103083A (en) * | 2017-12-13 | 2018-06-01 | 江苏省原子医学研究所 | Nucleotide sequence, expression vector, engineering bacteria and the production recombined human aldolase C method of encoding recombinant human's aldolase C |
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